O06745 (YITJ_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 81.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase | ||||
| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 612 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | S-methyl-L-methionine + L-homocysteine = 2 L-methionine. 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H. |
| Cofactor | FAD By similarity. Zinc Potential. |
| Pathway | |
| Induction | Induced by methionine starvation. Ref.3 |
| Sequence similarities | In the C-terminal section; belongs to the methylenetetrahydrofolate reductase family. Contains 1 Hcy-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Methionine biosynthesis |
| Ligand | FAD Flavoprotein Metal-binding NAD NADP S-adenosyl-L-methionine Zinc |
| Molecular function | Methyltransferase Oxidoreductase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversionInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW methylenetetrahydrofolate reductase (NADPH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 612 | 612 | Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase | PRO_0000379125 | |||||
Regions | |||||||||
| Domain | 1 – 280 | 280 | Hcy-binding | ||||||
| Region | 1 – 280 | 280 | Homocysteine S-methyltransferase | ||||||
| Region | 295 – 612 | 318 | 5,10-methylenetetrahydrofolate reductase | ||||||
Sites | |||||||||
| Metal binding | 200 | 1 | Zinc Potential | ||||||
| Metal binding | 265 | 1 | Zinc Potential | ||||||
| Metal binding | 266 | 1 | Zinc Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees position encoding 11 membrane proteins." Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J. Microbiology 143:3309-3312(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in Gram-positive bacteria." Grundy F.J., Henkin T.M. Mol. Microbiol. 30:737-749(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: 168 / BR151. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y09476 Genomic DNA. Translation: CAA70665.1. AL009126 Genomic DNA. Translation: CAB12941.1. |
| PIR | C69840. |
| RefSeq | NP_388982.1. NC_000964.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1UMY based on UniProtKB O09171. |
| ProteinModelPortal | O06745. |
| SMR | O06745. Positions 2-393. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU11010. |
Proteomic databases | |
| PaxDb | O06745. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12941; CAB12941; BSU11010. |
| GeneID | 939796. |
| KEGG | bsu:BSU11010. |
| PATRIC | 18973908. VBIBacSub10457_1148. |
Organism-specific databases | |
| GenoList | BSU11010. |
Phylogenomic databases | |
| eggNOG | COG0685. |
| HOGENOM | HOG000028409. |
| KO | K00547. |
| OMA | QSHLMGL. |
| ProtClustDB | PRK08645. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU11010-MONOMER. |
| UniPathway | UPA00193. |
Family and domain databases | |
| Gene3D | 3.20.20.330. 1 hit. |
| InterPro | IPR003171. Mehydrof_redctse. IPR003726. S_MeTrfase. [Graphical view] |
| Pfam | PF02219. MTHFR. 1 hit. PF02574. S-methyl_trans. 1 hit. [Graphical view] |
| SUPFAM | SSF82282. S_methyl_trans. 1 hit. |
| PROSITE | PS50970. HCY. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | YITJ_BACSU | ||||||||
| Accession | Primary (citable) accession number: O06745 Secondary accession number(s): Q796P9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
